Home
Resources
Publications
Inhibition of Calpain in Intact Platelets by the Thiol Protease Inhibitor E-64d

Inhibition of Calpain in Intact Platelets by the Thiol Protease Inhibitor E-64d

E B McGowan, E Becker, T C Detwiler

Biochem Biophys Res Commun. 1989 Jan 31;158(2):432-5.

PMID: 2537073

Abstract:

E-64d, a membrane permeant derivative of E-64c, a thiol protease inhibitor (Tamai et al. (1986) J. Pharmacobio-Dyn. 9, 672-677), was tested for ability to inhibit calpain activity in intact platelets. Calpain activity was measured by proteolysis of actin-binding protein and talin, two known substrates of calpain. Incubation of platelets with E-64c (not permeant) or E-64d before lysis prevented proteolysis after lysis. When the platelets were incubated with E-64c or E-64d and then washed to remove the drugs before lysis, only E-64d inhibited proteolysis. When platelets were incubated with E-64c or E-64d and then activated with A23187 plus calcium, a treatment that activates intraplatelet calpain, only E-64d inhibited proteolysis. These results indicate that E-64d can enter the intact cell and inhibit calpain.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP88321099-A	E-64d		88321-09-9	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: